Kinetic study of the interaction of oxy- and deoxyhemoglobins with the erythrocyte membrane. | Zendy

Nurith Shaklai | Zendy; Vandna Sharma | Zendy

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Kinetic study of the interaction of oxy- and deoxyhemoglobins with the erythrocyte membrane.

Author(s) -

Nurith Shaklai,

Vandna Sharma

Publication year - 1980

Publication title -

proceedings of the national academy of sciences

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.011

H-Index - 771

eISSN - 1091-6490

pISSN - 0027-8424

DOI - 10.1073/pnas.77.12.7147

Subject(s) - kinetics , chemistry , membrane , reaction rate constant , dissociation constant , receptor–ligand kinetics , hemoglobin , dissociation (chemistry) , biophysics , erythrocyte membrane , fluorescence , stopped flow , dissociation rate , biochemistry , biology , physics , receptor , quantum mechanics

Changes in fluorescence intensity of a membrane-embedded probe were used to study the kinetics of binding of oxy- and deoxyhemoglobin to erythrocyte membranes. For these studies, stopped-flow fluorimetric techniques were utilized. Both binding and dissociation of hemoglobin from membranes followed heterogeneous first-order kinetics. The rate constants for binding of oxyhemoglobin were about 10 times larger than those of deoxyhemoglobin; the dissociation rate constants of oxyhemoglobin were about one-quarter those of the unliganded form. The results are discussed in light of the steady-state binding constants previously derived for both oxy- and deoxyhemoglobin.

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